TABLE 1. Purification of PPIP5K from rat brain.
The enzyme was purified as described in Figs. 3 and 4 and assayed under first-order conditions (k-1 is the first-order rate constant). The data for -fold purification and % recovery should be considered approximate because the enzyme co-purifies with an inhibitor (probably InsP6; see “Results” for details). Purification parameters for the native gel electrophoresis experiment are not available as the protein concentration in each gel slice was not determined.
Protein | Volume | Total activity | Specific activity | Purification | Recovery | |
---|---|---|---|---|---|---|
mg/ml | ml | k-1/mg/min | k-1/mg/min | -fold | % | |
Supernatant | 4.2 | 160 | 1,632 | 2.4 | 1 | 100 |
DEAE | 1.2 | 193 | 1060 | 4.6 | 2 | 65 |
Heparin | 0.075 | 60 | 653 | 145 | 60 | 40 |
Ni | 0.1 | 9 | 870 | 967 | 402 | 53 |
Sucrose | 0.04 | 3 | 429 | 3575 | 1490 | 26 |